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Database: UniProt
Entry: Q97SH4
LinkDB: Q97SH4
Original site: Q97SH4 
ID   PTMCB_STRPN             Reviewed;         589 AA.
AC   Q97SH4;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   02-NOV-2016, entry version 102.
DE   RecName: Full=PTS system mannitol-specific EIICB component {ECO:0000250|UniProtKB:P28008};
DE   AltName: Full=EIICB-Mtl {ECO:0000250|UniProtKB:P28008};
DE            Short=EII-Mtl {ECO:0000250|UniProtKB:P28008};
DE   Includes:
DE     RecName: Full=Mannitol permease IIC component {ECO:0000250|UniProtKB:P28008};
DE     AltName: Full=PTS system mannitol-specific EIIC component {ECO:0000250|UniProtKB:P28008};
DE   Includes:
DE     RecName: Full=Mannitol-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P28008};
DE              EC=2.7.1.197 {ECO:0000250|UniProtKB:P00550, ECO:0000250|UniProtKB:P28008};
DE     AltName: Full=PTS system mannitol-specific EIIB component {ECO:0000250|UniProtKB:P28008};
GN   Name=mtlA; OrderedLocusNames=SP_0394;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T.,
RA   Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C.,
RA   Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar
CC       phosphotransferase system (sugar PTS), a major carbohydrate active
CC       transport system, catalyzes the phosphorylation of incoming sugar
CC       substrates concomitantly with their translocation across the cell
CC       membrane. The enzyme II CmtAB PTS system is involved in D-mannitol
CC       transport. {ECO:0000250|UniProtKB:P28008}.
CC   -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + D-
CC       mannitol(Side 1) = [protein]-L-histidine + D-mannitol 1-
CC       phosphate(Side 2). {ECO:0000250|UniProtKB:P00550,
CC       ECO:0000250|UniProtKB:P28008}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P28008}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00427}; Multi-pass membrane protein
CC       {ECO:0000255|PROSITE-ProRule:PRU00427}.
CC   -!- DOMAIN: The EIIC type-2 domain forms the PTS system translocation
CC       channel and contains the specific substrate-binding site.
CC       {ECO:0000255|PROSITE-ProRule:PRU00427}.
CC   -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-
CC       EIIA on a cysteinyl residue. Then, it transfers the phosphoryl
CC       group to the sugar substrate concomitantly with the sugar uptake
CC       processed by the PTS EIIC type-2 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00422}.
CC   -!- SIMILARITY: Contains 1 PTS EIIB type-2 domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC   -!- SIMILARITY: Contains 1 PTS EIIC type-2 domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00427}.
DR   EMBL; AE005672; AAK74558.1; -; Genomic_DNA.
DR   PIR; E95045; E95045.
DR   RefSeq; WP_000391672.1; NZ_AKVY01000001.1.
DR   ProteinModelPortal; Q97SH4; -.
DR   STRING; 170187.SP_0394; -.
DR   EnsemblBacteria; AAK74558; AAK74558; SP_0394.
DR   KEGG; spn:SP_0394; -.
DR   PATRIC; 19705137; VBIStrPne105772_0414.
DR   eggNOG; ENOG4105CTS; Bacteria.
DR   eggNOG; COG2213; LUCA.
DR   HOGENOM; HOG000252814; -.
DR   KO; K02799; -.
DR   KO; K02800; -.
DR   OMA; GWAIKRF; -.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0022872; F:protein-N(PI)-phosphohistidine-mannitol phosphotransferase system transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   CDD; cd05567; PTS_IIB_mannitol; 2.
DR   Gene3D; 3.40.50.10370; -; 2.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR003501; PTS_EIIB_2/3.
DR   InterPro; IPR029503; PTS_EIIB_mannitol.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   InterPro; IPR004718; PTS_IIC_mtl.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF52794; SSF52794; 2.
DR   TIGRFAMs; TIGR00851; mtlA; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Kinase; Membrane; Phosphoprotein;
KW   Phosphotransferase system; Sugar transport; Transferase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    589       PTS system mannitol-specific EIICB
FT                                component.
FT                                /FTId=PRO_0000186630.
FT   TOPO_DOM      1     25       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM     26     47       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM     48     51       Extracellular.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM     52     72       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM     73    135       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    136    157       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    158    166       Extracellular.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    167    187       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    188    274       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    275    294       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    295    316       Extracellular.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    317    338       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    339    589       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   DOMAIN       14    347       PTS EIIC type-2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   DOMAIN      381    476       PTS EIIB type-2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00422}.
FT   ACT_SITE    387    387       Phosphocysteine intermediate; for EIIB
FT                                activity. {ECO:0000250|UniProtKB:P00550,
FT                                ECO:0000250|UniProtKB:P28008}.
FT   MOD_RES     387    387       Phosphocysteine; by EIIA.
FT                                {ECO:0000250|UniProtKB:P00550,
FT                                ECO:0000250|UniProtKB:P28008,
FT                                ECO:0000255|PROSITE-ProRule:PRU00422}.
SQ   SEQUENCE   589 AA;  61855 MW;  A7F565D63682DC97 CRC64;
     MEEKVSLKVR VQKLGTSLSN MVMPNIGAFI AWGVLTALFI ADGYLPNEQL ATVVGPMLTY
     LLPILIGYTG GYMIHGQRGA VVGAIATVGA ITGSSVPMFI GAMVMGPLGG WTIKKFDEKF
     QEKIRPGFEM LVNNFSAGLV GFALLLLAFY AIGPVVSTLT GAVGNGVEAI VNARLLPMAN
     IIIEPAKVLF LNNALNHGIF TPLGVEQVAQ AGKSILFLLE ANPGPGLGIL LAYAVFGKGS
     AKSSSWGAMV IHFFGGIHEI YFPYVMMKPT LFLAAMAGGI SGTFTFQLLD AGLKSPASPG
     SIIAIIATAP KGVWPHLNVL LGVLVAAVVS FLVAALILHA DKSTEDSLEA AQAATQAAKA
     QSKGQLVSTS VDAVVSTDSV EKIIFACDAG MGSSAMGASI LRDKVKKAGL EIPVSNQAIS
     NLLDTPKTLI VTQEELTPRA KDKSPSAIHV SVDNFLASSR YDEIVASLTG ASPIAEIEGD
     IPTSAPVDSQ ESDLNHIDAV VVAYGKAQGT ATMGCETIRA IFRNKNIRIP VSTAKISELG
     EFNSKNIMIV TTISLQAEVQ QAAPNSQFLI VDSLVTTPEY DKMAARMYK
//
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